Involvement of cysteine residues in the electrophoretic mobility of histone H3 in acid-urea-Triton gels.
Carbamylation of cysteines 96 and 110 in histone H3 increases the electrophoretic mobility of this histone in acetic acid-urea-Triton X-100 polyacrylamide gels but has no effect in gels lacking Triton. Residue 96 appears to be a major determinant in the affinity of histone H3 for the nonionic detergent Triton. Carbamylation and carboxymethylation of cysteine 96 caused a major loss of the gel retardation caused by Triton. Carbamylation of cysteine 110 did not affect Triton binding but prevented ionization of the thiol side-chain moiety in the acetic acid-urea-Triton X-100 gel.
Waterborg
J H
JH
Division of Cell Biology and Biophysics, School of Basic Life Sciences, University of Missouri, Kansas City 64110-2499.
D000107:Acetylation; D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000737:chemistry; D003545:Cysteine / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D014644:Genetic Variation; D006657:Histones / Q000737:chemistry*; D000455:Medicago sativa / Q000032:analysis; D008745:Methylation; D017830:Octoxynol; D011092:Polyethylene Glycols; D014508:Urea
D006657:Histones; D011092:Polyethylene Glycols; D014508:Urea; D017830:Octoxynol; D003545:Cysteine